Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2PPA

Anaerobically manipulated wild type oxidized AfNiR bound to nitrous oxide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
A	0016491	molecular_function	oxidoreductase activity
A	0019333	biological_process	denitrification pathway
A	0042128	biological_process	nitrate assimilation
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding
A	0050421	molecular_function	nitrite reductase (NO-forming) activity
B	0005507	molecular_function	copper ion binding
B	0016491	molecular_function	oxidoreductase activity
B	0019333	biological_process	denitrification pathway
B	0042128	biological_process	nitrate assimilation
B	0042597	cellular_component	periplasmic space
B	0046872	molecular_function	metal ion binding
B	0050421	molecular_function	nitrite reductase (NO-forming) activity
C	0005507	molecular_function	copper ion binding
C	0016491	molecular_function	oxidoreductase activity
C	0019333	biological_process	denitrification pathway
C	0042128	biological_process	nitrate assimilation
C	0042597	cellular_component	periplasmic space
C	0046872	molecular_function	metal ion binding
C	0050421	molecular_function	nitrite reductase (NO-forming) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU1 A 501

Chain	Residue
A	HIS95
A	CYS136
A	HIS145
A	MET150

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU A 502

Chain	Residue
A	HIS100
A	HIS135
B	HIS306

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU1 B 501

Chain	Residue
B	HIS145
B	MET150
B	HIS95
B	CYS136

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU B 502

Chain	Residue
B	HIS100
B	HIS135
C	HIS306

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU1 C 501

Chain	Residue
C	HIS95
C	CYS136
C	HIS145
C	MET150

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU C 502

Chain	Residue
A	HIS306
C	HIS100
C	HIS135

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACT C 503

Chain	Residue
A	ILE257
A	HIS306
A	LEU308
C	ASP98
C	HIS100
C	HIS135
C	ALA137
C	HOH1593

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACT C 1502

Chain	Residue
A	ALA302
C	HOH1597

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT B 1503

Chain	Residue
B	GLY229
B	ILE300
B	HIS319
B	HOH1722

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT B 1504

Chain	Residue
A	GLU113
A	HOH1549
B	ASP173
B	GLY238
B	GLU239
B	LYS240
B	HOH1553

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT B 1505

Chain	Residue
B	GLY140
B	MET141
B	PRO143
B	TRP144
C	GLU313

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT C 1506

Chain	Residue
A	HOH1635
B	PHE282
C	PHE282
C	HOH1623
C	HOH1643
C	HOH1665
C	HOH1728

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT C 1507

Chain	Residue
C	HIS60
C	TYR184
C	THR206
C	HOH1547
C	HOH1601

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT C 1508

Chain	Residue
A	GLU313
C	GLY140
C	MET141
C	PRO143
C	TRP144
C	MET210

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT C 1509

Chain	Residue
C	GLY229
C	ILE300
C	HIS319
C	LYS321

site_id	BC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACT A 1510

Chain	Residue
A	GLY140
A	MET141
A	PRO143
A	TRP144
A	TYR203
A	MET210
B	GLU313
B	GLU325

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE N2O A 503

Chain	Residue
A	HIS100
A	HIS135
A	HOH1601
B	ILE257
B	HIS306
B	LEU308

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE N2O B 503

Chain	Residue
B	HIS100
B	HIS135
B	HOH1556
C	ILE257
C	HIS306
C	LEU308

site_id	CC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE TRS A 1501

Chain	Residue
C	LEU213
C	THR214
A	THR212
A	LEU213
A	THR214
A	HOH1687
A	HOH1704
A	HOH1708
B	THR212
B	LEU213
B	THR214
C	THR212

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Binding site: {"description":"type 1 copper site","evidences":[{"source":"PubMed","id":"8172899","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"description":"type 2 copper site"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	9
Details	Binding site: {"description":"type 1 copper site"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {"description":"type 2 copper site","evidences":[{"source":"PubMed","id":"8172899","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	164
Details	Domain: {"description":"Plastocyanin-like 2"}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
A	ASP98
A	HIS255

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
B	ASP98
B	HIS255

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
C	ASP98
C	HIS255

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)